Title : Intrinsic tryptophans of CRABPI as probes of structure and folding.

Pub. Date : 1996 Jun

PMID : 8762142






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The native state fluorescence and CD spectra of the predominantly beta-sheet cellular retinoic acid-binding protein I (CRABPI) include contributions from its three tryptophan residues and are influenced by the positions of these residues in the three-dimensional structure. Cadmium cellular retinoic acid binding protein 1 Homo sapiens
2 Although the far-UV CD spectrum of CRABPI is largely determined by the protein"s secondary structure, aromatic clustering around Trp 87 and the aromatic-charge interaction between Arg 111 and Trp 109 give rise to a characteristic feature in the CD spectrum at 228 nm. Cadmium cellular retinoic acid binding protein 1 Homo sapiens